This investigation will be concerned with the mechanism of hydrolysis of acetals and acetal analogues to gain information regarding the chemical possibilities by which glycosidic enzymes might be acting. The structural features in acetals that will allow and facilitate both bimolecular and intramolecular general acid catalysis will be determined. It will be the purpose of this investigation to demonstrate these mechanistic possibilities in non-enzymatic systems, and to assess completely the mechanism of action of glycosidic enzymes such as lysozyme by analogy to the chemical models and by direct comparison of enzyme and chemical experiments. Kinetic studies on an extensive series of acetals and acetal analogues will be carried out to determine quantitatively the relative importance of structural features such as basicity, carbonium ion stability and leaving group abillity in leading to concerted general acid catalysis. These compounds are idealy suited for in-depth mechanism studies of general acid catalyzed reactions in which structure-reactivity relationships can be obtained to ascertain the factors responsible for general acid catalysis, and it will be possible thereby to rigorously establish transition state structure in reactions of these compounds. Kinetic experiments on glycosidic enzymes with synthetically prepared substrates to answer specific questions such as the importance of nucleophilic participation and strain effects should allow elucidation of the detailed mechanistic pathways of the enzymatic reaction. In conjunction with the chemical model studies these studies should then allow understanding of the mechanism and the rate constants in the enzymatic reactions in chemical terms.